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Matei Bolborea, Gisela Helfer, Francis J P Ebling, and Perry Barrett

cyclase is a signal transduction pathway commonly associated with TSH receptor activation, but TSH receptors are known to couple with a diverse range of G proteins to activate several different pathways that potentially have multiple downstream

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M Hołysz, N Derebecka-Hołysz, and W H Trzeciak

( Trzeciak & Boyd 1974 , Boyd et al . 1975 ). ACTH binds to a specific receptor coupled with membrane-bound adenylyl cyclase; thus, cAMP is generated and activates the protein kinase A (PKA) signal transduction pathway, which leads to phosphorylation and

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Baowei Jiao, Xigui Huang, Chi Bun Chan, Li Zhang, Deshou Wang, and Christopher H K Cheng

substituted by an YXXFS motif. In addition, there are two conserved regions within the intracellular domain termed Box 1 and Box 2 that are important for signal transduction of the receptor. The proline-rich Box 1 region is the site of Janus kinase 2 (JAK2

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Gábor Turu and László Hunyady

this review is to discuss the intracellular mechanisms of the action of CB 1 R. After summarizing the available data about the G-protein activation and signal transduction of CB 1 R, this review also analyses recent data about dimerization or

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Gerald Thiel, Isabelle Müller, and Oliver G Rössler

Islam MS 2011 TRP channels of islets. In: Transient receptor potential channels. Advances in Experimental Medicine and Biology 704 811–830 (Fig. 42.1) with kind permission from Springer Science+Business Media B.V.). Figure 3 Signal transduction of

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N Martínez-Micaelo, N González-Abuín, A Ardévol, M Pinent, E Petretto, J Behmoaras, and M Blay

consequence of a differential regulation of the leptin signalling pathway genes, the expression of key genes involved in the regulation of leptin signal transduction in relevant organs, including the mesenteric fat pad, the hypothalamus and the liver was

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Marta Labeur, Barbara Wölfel, Johanna Stalla, and Günter K Stalla

and as RA, a CRH signaling pathway inhibitor, may modulate TMEFF2, we decided to investigate in detail the effects of TMEFF2 on the signal transduction pathway of CRH. Materials and methods Cell culture and chemicals AtT20 pituitary corticotrope tumor

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Hong Zhou, Yonghua Jiang, Wendy K W Ko, Wensheng Li, and Anderson O L Wong

. Furthermore, we also speculate that (i) the JAK2/MAPK cascades secondary coupled to the cAMP-dependent pathway and (ii) the PI3K cascade independent of cAMP-mediated mechanisms may be the key elements in the signal transduction for LH-induced GH gene

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Fabiana Cornejo Maciel, Paula Maloberti, Isabel Neuman, Florencia Cano, Rocío Castilla, Fernanda Castillo, Cristina Paz, and Ernesto J Podestá

–45 min) proved to modify the intracellular content of MTE-I (data not shown). However, ACTH produces an increase of ACS4 levels evaluated by Western blot. Analysis of the intensity of ACS4 signal demonstrated that ACTH (10 mIU/ml) induces ACS4 levels to

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C Bignon, N Daniel, L Belair, and J Djiane

The recent finding that sheep had long (l-oPRLR) and short (s-oPRLR) prolactin receptors provided new tools to further explore prolactin signaling to target genes. Here we used CHO cells transfected with l-oPRLR or s-oPRLR cDNAs to compare the activation of known key steps of prolactin signaling by the two receptors. We found that prolactin stimulated l-oPRLR tyrosine phosphorylation, although it lacked the last tyrosine residue found in other long prolactin receptors. In addition, l-oPRLR and s-oPRLR both responded to prolactin stimulation by (1) Janus kinase 2 (Jak2) tyrosine phosphorylation, (2) DNA-binding activation of signal transducer and activator of transcription 5 (STAT5), (3) stimulation of transcription from a promoter made of six repeats of STAT5-responsive sequence. However, although it contains STAT5-binding consensus sequences, the ovine beta-lactoglobulin promoter (-4000 to +40) was transactivated by l-oPRLR, but not by s-oPRLR. Taken together, our results indicate that activation of Jak2/STAT5 pathway alone is not sufficient to account for prolactin-induced transcription of this milk protein gene, and that sequences of its promoter, other than STAT5-specific sequences, account for the opposite transcriptional activation capabilities of l-oPRLR and s-oPRLR.